Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits.
about
Structure of the T109S mutant ofEscherichia colidihydroorotase complexed with the inhibitor 5-fluoroorotate: catalytic activity is reflected by the crystal formDihydroorotase from the Hyperthermophile Aquifiex aeolicus Is Activated by Stoichiometric Association with Aspartate Transcarbamoylase and Forms a One-Pot Reactor for Pyrimidine Biosynthesis † ‡Structure of dihydroorotase fromBacillus anthracisat 2.6 Å resolutionAtomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenaseCa-asp bound X-ray structure and inhibition of Bacillus anthracis dihydroorotase (DHOase).Expression, purification, crystallization and preliminary X-ray diffraction analysis of the dihydroorotase domain of human CAD.Intersubunit communication in the dihydroorotase-aspartate transcarbamoylase complex of Aquifex aeolicus.Ultrasensitive regulation of anapleurosis via allosteric activation of PEP carboxylase.
P2860
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P2860
Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits.
description
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name
Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits.
@en
Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits.
@nl
type
label
Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits.
@en
Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits.
@nl
prefLabel
Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits.
@en
Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits.
@nl
P2093
P1476
Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits
@en
P2093
Camilla W Chan
J Mitchell Guss
Richard I Christopherson
P304
P356
10.1016/J.JMB.2005.01.067
P407
P577
2005-05-01T00:00:00Z